CDK5_BOVIN
ID CDK5_BOVIN Reviewed; 292 AA.
AC Q02399; Q0VCN5; Q6LBE2;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Cyclin-dependent kinase 5 {ECO:0000250|UniProtKB:Q00535};
DE EC=2.7.11.1;
DE AltName: Full=Cell division protein kinase 5 {ECO:0000305};
DE AltName: Full=Cyclin-dependent-like kinase 5;
DE AltName: Full=Proline-directed protein kinase 33 kDa subunit {ECO:0000303|PubMed:1464604};
DE Short=PDPK {ECO:0000303|PubMed:1464604};
DE AltName: Full=Serine/threonine-protein kinase PSSALRE {ECO:0000250|UniProtKB:Q03114};
DE AltName: Full=Tau protein kinase II catalytic subunit {ECO:0000303|PubMed:8253190};
DE Short=TPKII catalytic subunit {ECO:0000303|PubMed:8253190};
GN Name=CDK5 {ECO:0000250|UniProtKB:Q00535};
GN Synonyms=CDKN5 {ECO:0000250|UniProtKB:Q00535},
GN PSSALRE {ECO:0000250|UniProtKB:P49615};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 14-20 AND 218-251.
RC TISSUE=Brain;
RX PubMed=1464604; DOI=10.1016/s0021-9258(18)35696-5;
RA Lew J., Winkfein R.J., Paudel H.K., Wang J.H.;
RT "Brain proline-directed protein kinase is a neurofilament kinase which
RT displays high sequence homology to p34cdc2.";
RL J. Biol. Chem. 267:25922-25926(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8253190; DOI=10.1016/0014-5793(93)80723-8;
RA Kobayashi S., Ishiguro K., Omori A., Takamatsu M., Arioka M., Imahori K.,
RA Uchida T.;
RT "A cdc2-related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit
RT of tau protein kinase II, a proline-directed protein kinase associated with
RT microtubule.";
RL FEBS Lett. 335:171-175(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Proline-directed serine/threonine-protein kinase essential
CC for neuronal cell cycle arrest and differentiation and may be involved
CC in apoptotic cell death in neuronal diseases by triggering abortive
CC cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins.
CC Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1,
CC SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16,
CC RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53,
CC HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM.
CC Regulates several neuronal development and physiological processes
CC including neuronal survival, migration and differentiation, axonal and
CC neurite growth, synaptogenesis, oligodendrocyte differentiation,
CC synaptic plasticity and neurotransmission, by phosphorylating key
CC proteins. Negatively regulates the CACNA1B/CAV2.2 -mediated Ca(2+)
CC release probability at hippocampal neuronal soma and synaptic terminals
CC (By similarity). Activated by interaction with CDK5R1 (p35) and CDK5R2
CC (p39), especially in postmitotic neurons, and promotes CDK5R1 (p35)
CC expression in an autostimulation loop. Phosphorylates many downstream
CC substrates such as Rho and Ras family small GTPases (e.g. PAK1, RAC1,
CC RHOA, CDC42) or microtubule-binding proteins (e.g. MAPT/TAU, MAP2,
CC MAP1B), and modulates actin dynamics to regulate neurite growth and/or
CC spine morphogenesis. Phosphorylates also exocytosis associated proteins
CC such as MCAM/MUC18, SEPT5, SYN1, and CDK16/PCTAIRE1 as well as
CC endocytosis associated proteins such as DNM1, AMPH and SYNJ1 at
CC synaptic terminals. In the mature central nervous system (CNS),
CC regulates neurotransmitter movements by phosphorylating substrates
CC associated with neurotransmitter release and synapse plasticity;
CC synaptic vesicle exocytosis, vesicles fusion with the presynaptic
CC membrane, and endocytosis. Promotes cell survival by activating anti-
CC apoptotic proteins BCL2 and STAT3, and negatively regulating of
CC JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to
CC genotoxic and oxidative stresses enhances its stabilization by
CC preventing ubiquitin ligase-mediated proteasomal degradation, and
CC induces transactivation of p53/TP53 target genes, thus regulating
CC apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by
CC preventing calpain-mediated proteolysis producing p25/CDK5R1 and
CC avoiding ubiquitin ligase-mediated proteasomal degradation. During
CC aberrant cell-cycle activity and DNA damage, p25/CDK5 activity elicits
CC cell-cycle activity and double-strand DNA breaks that precedes neuronal
CC death by deregulating HDAC1. DNA damage triggered phosphorylation of
CC huntingtin/HTT in nuclei of neurons protects neurons against
CC polyglutamine expansion as well as DNA damage mediated toxicity.
CC Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in
CC matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs)
CC differentiation. Negative regulator of Wnt/beta-catenin signaling
CC pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of
CC translation) pathway, which suppresses expression of a post-
CC transcriptional regulon of proinflammatory genes in myeloid cells;
CC phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase
CC (EPRS) in a IFN-gamma-dependent manner, the initial event in assembly
CC of the GAIT complex. Phosphorylation of SH3GLB1 is required for
CC autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5
CC in response to osmotic stress mediates its rapid nuclear localization.
CC MEF2 is inactivated by phosphorylation in nucleus in response to
CC neurotoxin, thus leading to neuronal apoptosis. APEX1 AP-
CC endodeoxyribonuclease is repressed by phosphorylation, resulting in
CC accumulation of DNA damage and contributing to neuronal death. NOS3
CC phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC
CC phosphorylation mediates its ubiquitin-dependent degradation and thus
CC leads to cytoskeletal reorganization. May regulate endothelial cell
CC migration and angiogenesis via the modulation of lamellipodia
CC formation. Involved in dendritic spine morphogenesis by mediating the
CC EFNA1-EPHA4 signaling. The complex p35/CDK5 participates in the
CC regulation of the circadian clock by modulating the function of CLOCK
CC protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates
CC the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in
CC association with altered stability and subcellular distribution (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q03114}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Inhibited by 2-(1-ethyl-2-hydroxyethylamino)-6-
CC benzylamino-9-isopropylpurine (roscovitine), 1-isopropyl-4-aminobenzyl-
CC 6-ether-linked benzimidazoles, resveratrol, AT-7519 and olomoucine.
CC Activated by CDK5R1 (p35) and CDK5R2 (p39) during the development of
CC the nervous system; degradation of CDK5R1 (p35) and CDK5R2 (p39) by
CC proteasome result in down regulation of kinase activity, during this
CC process, CDK5 phosphorylates p35 and induces its ubiquitination and
CC subsequent degradation. Kinase activity is mainly determined by the
CC amount of p35 available and subcellular location; reversible
CC association to plasma membrane inhibits activity. Long-term
CC inactivation as well as CDK5R1 (p25)-mediated hyperactivation of CDK5
CC triggers cell death. The pro-death activity of hyperactivated CDK5 is
CC suppressed by membrane association of CDK5, via myristoylation of p35.
CC Brain-derived neurotrophic factor, glial-derived neurotrophic factor,
CC nerve growth factor (NGF), retinoic acid, laminin and neuregulin
CC promote activity. Neurotoxicity enhances nuclear activity, thus leading
CC to MEF2 phosphorylation and inhibition prior to apoptosis of cortical
CC neurons. Repression by GSTP1 via p25/p35 translocation prevents
CC neurodegeneration (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer composed of a catalytic subunit CDK5 and a
CC regulatory subunit CDK5R1 (p25) and macromolecular complex composed of
CC at least CDK5, CDK5R1 (p35) and CDK5RAP1 or CDK5RAP2 or CDK5RAP3. Only
CC the heterodimer shows kinase activity. Under neurotoxic stress and
CC neuronal injury conditions, p35 is cleaved by calpain to generate p25
CC that hyperactivates CDK5, that becomes functionally disabled and often
CC toxic. Found in a trimolecular complex with CABLES1 and ABL1. Interacts
CC with CABLES1 and CABLES2 (By similarity). Interacts with AATK and
CC GSTP1. Binds to HDAC1 when in complex with p25. Interaction with
CC myristoylation p35 promotes CDK5 association with membranes. Both
CC isoforms 1 and 2 interacts with beta-catenin/CTNNB1. Interacts with
CC delta-catenin/CTNND2 and APEX1. Interacts with P53/TP53 in neurons (By
CC similarity). Interacts with EPHA4; may mediate the activation of NGEF
CC by EPHA4. Interacts with PTK2/FAK1. The complex p35/CDK5 interacts with
CC CLOCK (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q00535}. Cytoplasm
CC {ECO:0000250|UniProtKB:P49615}. Cell membrane
CC {ECO:0000250|UniProtKB:Q00535}; Peripheral membrane protein
CC {ECO:0000250}. Perikaryon {ECO:0000250}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:P49615}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P49615}. Nucleus {ECO:0000250}. Postsynaptic
CC density {ECO:0000250|UniProtKB:Q03114}. Synapse
CC {ECO:0000250|UniProtKB:Q03114}. Note=In axonal growth cone with
CC extension to the peripheral lamellipodia (By similarity). Under
CC neurotoxic stress and neuronal injury conditions, CDK5R1 (p35) is
CC cleaved by calpain to generate CDK5R1 (p25) in response to increased
CC intracellular calcium. The elevated level of p25, when in complex with
CC CDK5, leads to its subcellular misallocation as well as its
CC hyperactivation. Colocalizes with CTNND2 in the cell body of neuronal
CC cells, and with CTNNB1 in the cell-cell contacts and plasma membrane of
CC undifferentiated and differentiated neuroblastoma cells. Reversibly
CC attached to the plasma membrane in an inactive form when complexed to
CC dephosphorylated p35 or CDK5R2 (p39), p35 phosphorylation releases this
CC attachment and activates CDK5 (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation on Tyr-15 by ABL1 and FYN, and on Ser-159 by
CC casein kinase 1 promotes kinase activity. By contrast, phosphorylation
CC at Thr-14 inhibits activity (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-159 is essential for maximal catalytic
CC activity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; L04798; AAA30606.1; -; mRNA.
DR EMBL; X82440; CAA57821.1; -; mRNA.
DR EMBL; BC120083; AAI20084.1; -; mRNA.
DR RefSeq; NP_776442.1; NM_174017.2.
DR AlphaFoldDB; Q02399; -.
DR SMR; Q02399; -.
DR BioGRID; 158435; 2.
DR CORUM; Q02399; -.
DR IntAct; Q02399; 3.
DR STRING; 9913.ENSBTAP00000010212; -.
DR iPTMnet; Q02399; -.
DR PaxDb; Q02399; -.
DR PRIDE; Q02399; -.
DR Ensembl; ENSBTAT00000010212; ENSBTAP00000010212; ENSBTAG00000007766.
DR GeneID; 281066; -.
DR KEGG; bta:281066; -.
DR CTD; 1020; -.
DR VEuPathDB; HostDB:ENSBTAG00000007766; -.
DR VGNC; VGNC:27127; CDK5.
DR eggNOG; KOG0662; Eukaryota.
DR GeneTree; ENSGT00940000160805; -.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q02399; -.
DR OMA; QHPWFND; -.
DR OrthoDB; 1010560at2759; -.
DR TreeFam; TF101023; -.
DR BRENDA; 2.7.11.22; 908.
DR Reactome; R-BTA-399956; CRMPs in Sema3A signaling.
DR Reactome; R-BTA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000007766; Expressed in oocyte and 105 other tissues.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:AgBase.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0005829; C:cytosol; ISS:AgBase.
DR GO; GO:0030425; C:dendrite; ISS:AgBase.
DR GO; GO:0030175; C:filopodium; ISS:AgBase.
DR GO; GO:0030426; C:growth cone; ISS:AgBase.
DR GO; GO:0030027; C:lamellipodium; ISS:AgBase.
DR GO; GO:0016020; C:membrane; ISS:AgBase.
DR GO; GO:0031594; C:neuromuscular junction; ISS:AgBase.
DR GO; GO:0043025; C:neuronal cell body; ISS:AgBase.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:AgBase.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISS:UniProtKB.
DR GO; GO:0016533; C:protein kinase 5 complex; IEA:Ensembl.
DR GO; GO:0030549; F:acetylcholine receptor activator activity; ISS:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0005176; F:ErbB-2 class receptor binding; ISS:AgBase.
DR GO; GO:0043125; F:ErbB-3 class receptor binding; ISS:UniProtKB.
DR GO; GO:0035173; F:histone kinase activity; TAS:UniProtKB.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0016301; F:kinase activity; ISS:AgBase.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:AgBase.
DR GO; GO:0050321; F:tau-protein kinase activity; ISS:AgBase.
DR GO; GO:0007409; P:axonogenesis; ISS:AgBase.
DR GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
DR GO; GO:0070509; P:calcium ion import; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0016477; P:cell migration; ISS:AgBase.
DR GO; GO:0007160; P:cell-matrix adhesion; ISS:AgBase.
DR GO; GO:0021954; P:central nervous system neuron development; IEA:Ensembl.
DR GO; GO:0021697; P:cerebellar cortex formation; IEA:Ensembl.
DR GO; GO:0022038; P:corpus callosum development; IEA:Ensembl.
DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; IEA:Ensembl.
DR GO; GO:0021819; P:layer formation in cerebral cortex; IEA:Ensembl.
DR GO; GO:0008045; P:motor neuron axon guidance; IEA:Ensembl.
DR GO; GO:0030517; P:negative regulation of axon extension; IEA:Ensembl.
DR GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
DR GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
DR GO; GO:0046826; P:negative regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
DR GO; GO:0031914; P:negative regulation of synaptic plasticity; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; ISS:AgBase.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; ISS:AgBase.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IEA:Ensembl.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IEA:Ensembl.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IEA:Ensembl.
DR GO; GO:0035418; P:protein localization to synapse; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0032801; P:receptor catabolic process; IEA:Ensembl.
DR GO; GO:0043113; P:receptor clustering; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; ISS:AgBase.
DR GO; GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0014044; P:Schwann cell development; IEA:Ensembl.
DR GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
DR GO; GO:0042501; P:serine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; IEA:Ensembl.
DR GO; GO:0001963; P:synaptic transmission, dopaminergic; IEA:Ensembl.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IEA:Ensembl.
DR GO; GO:0048489; P:synaptic vesicle transport; IBA:GO_Central.
DR GO; GO:0008542; P:visual learning; IEA:Ensembl.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; ATP-binding; Biological rhythms; Cell cycle;
KW Cell division; Cell membrane; Cell projection; Cytoplasm;
KW Direct protein sequencing; Kinase; Membrane; Neurodegeneration;
KW Neurogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Synapse; Transferase.
FT CHAIN 1..292
FT /note="Cyclin-dependent kinase 5"
FT /id="PRO_0000085783"
FT DOMAIN 4..286
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 126
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 33
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 15
FT /note="Phosphotyrosine; by ABL1, EPHA4 and FYN"
FT /evidence="ECO:0000250|UniProtKB:Q00535"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00535"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q00535"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00535"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00535"
FT CONFLICT 61
FT /note="K -> E (in Ref. 3; AAI20084)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="F -> L (in Ref. 3; AAI20084)"
FT /evidence="ECO:0000305"
FT CONFLICT 169
FT /note="P -> S (in Ref. 1; AAA30606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 33288 MW; 4CB11CED9017D535 CRC64;
MQKYEKLEKI GEGTYGTVFK AKNRETHEIV ALKRVRLDDD DEGVPSSALR EICLLKELKH
KNIVRLHDVL HSDKKLTLVF EFCDQDLKKY FDSCNGDLDP EIVKSFLFQL LKGLGFCHSR
NVLHRDLKPQ NLLINRNGEL KLADFGLARA FGIPVRCYSA EVVTLWYRPP DVLFGAKLYS
TSIDMWSAGC IFAELANAGR PLFPGNDVDD QLKRIFRLLG TPTEEQWPAM TKLPDYKPYP
MYPATTSLVN VVPKLNATGR DLLQNLLKCN PVQRISAEEA LQHPYFSDFC PP
